Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03E83 (PUR9_PEDPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:PEPE_1458
OrganismPediococcus pentosaceus (strain ATCC 25745 / 183-1w) [Complete proteome] [HAMAP]
Taxonomic identifier278197 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaePediococcus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018922

Sequences

Sequence LengthMass (Da)Tools
Q03E83 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: B4020CBDB5383A91

FASTA51155,930
        10         20         30         40         50         60 
MKTALLSVSD KTGIVEFARG LVKADFRIIS TGGTKKVLEE AGLSIVSVEA ITNFPEMLDG 

        70         80         90        100        110        120 
RVKTLHPAIH GGLLARRDLP EHLAALKEHN IDLIDLVCVN LYPFKSTIMQ NGVTEAEAIE 

       130        140        150        160        170        180 
QIDIGGPSML RSAAKNFASV LPVVDPKDYQ PVLAALAHQT DNVKFRRALA LKVFQHTAAY 

       190        200        210        220        230        240 
DTLIAQYLGQ NGEIFPDELT KTYTKKQVMR YGENSHQKAA FYEDALPVPF SIAQAQQLHG 

       250        260        270        280        290        300 
KELSYNNIKD ADAALKMSAE FNQPAVVAVK HMNPCGIGLG QNIEEAWDRA YEADSMSIFG 

       310        320        330        340        350        360 
GIIVLNRPVD LATAEKMHKL FLEIIIAPSF EKEAFTVLAQ KKNLRIMTVD FNQHQDAKEL 

       370        380        390        400        410        420 
ETVSVMGGLL VQEQDAVVET ATDFKVVSKR QPTESELKAM VFGQTVVKHV KSNAIVITTD 

       430        440        450        460        470        480 
QQTLGIGAGQ MNRIGSVEIA VKQAEGSANF KNAVMASDAF FPMEDCVEYA AKHGIKAIVE 

       490        500        510 
PGGSIKDQAS IDKADELGIS LIFSGRRHFR H 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000422 Genomic DNA. Translation: ABJ68489.1.
RefSeqYP_804931.1. NC_008525.1.

3D structure databases

ProteinModelPortalQ03E83.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING278197.PEPE_1458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ68489; ABJ68489; PEPE_1458.
GeneID4417281.
KEGGppe:PEPE_1458.
PATRIC22876226. VBIPedPen34213_1375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycPPEN278197:GI4Y-1458-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_PEDPA
AccessionPrimary (citable) accession number: Q03E83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways